Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding.

The Journal of biological chemistry - 31 Dec 1999

Fivaz M, Velluz M C, van der Goot F G

Abstract excerpt

The pore-forming toxin aerolysin is secreted by Aeromonas hydrophila as an inactive precursor. Based on chemical cross-linking and gel filtration, we show here that proaerolysin exists as a monomer at low concentrations but is dimeric above 0.1 mg/ml. At intermediate concentrations, monomers and dimers appeared to be in rapid equilibrium. All together our data indicate that, at low concentrations, the toxin is a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Toxins
Share to Cell Line
Share to Chromatography, Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cricetinae

Share to Cross-Linking Reagents

Share to Dimerization

Share to Pore Forming Cytotoxic Proteins

Share to Receptors, Cell Surface

Source

Identifiers

PMID: 10608828
DOI: 10.1074/jbc.274.53.37705

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding.PMID 10608828Read ↗

The channel-forming protein proaerolysin remains a dimer at low concentrations in solution.Semantic proximity Read ↗

Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator.Semantic proximity Read ↗

Anthrax toxin receptor drives protective antigen oligomerization and stabilizes the heptameric and octameric oligomer by a similar mechanism.Semantic proximity Read ↗

The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding.Semantic proximity Read ↗

Identification of functional domains of Clostridium septicum alpha toxin.Semantic proximity Read ↗

Self-association of the transmembrane domain of an anthrax toxin receptor.Semantic proximity Read ↗

Site-directed mutagenesis of the hole-forming toxin aerolysin: studies on the roles of histidines in receptor binding and oligomerization of the monomer.Semantic proximity Read ↗

The channel-forming toxin aerolysin neutralizes human immunodeficiency virus type 1.Semantic proximity Read ↗

Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal alpha-toxin into the lipid bilayer.Semantic proximity Read ↗

In vivo detection of hetero-association of glycophorin-A and its mutants within the membrane.Semantic proximity Read ↗

Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax.Semantic proximity Read ↗

Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.